21.神経芽細胞腫肝転移例の1年生存(第589回千葉医学会例会・第2回千葉大学小児外科教室例会)

Additional file 2: Table S1. A list of phosphoPSMs identified by MASCOT and SEQUEST

MOESM1 of Phosphotyrosine profiling of curcumin-induced signaling

Additional file 1: Figure 1. (A) Cell viability of CAL 27 with indicated concentrations of curcumin. Classification of differentially phosphorylated proteins based on (B) Localization (C) Biological process (D) Molecular function

A Comprehensive Map of the Human Urinary Proteome

The study of the human urinary proteome has the potential to offer significant insights into normal physiology as well as disease pathology. The information obtained from such studies could be applied to the diagnosis of various diseases. The high sensitivity, resolution, and mass accuracy of the latest generation of mass spectrometers provides an opportunity to accurately catalog the proteins present in human urine, including those present at low levels. To this end, we carried out a comprehensive analysis of human urinary proteome from healthy individuals using high-resolution Fourier transform mass spectrometry. Importantly, we used the Orbitrap for detecting ions in both MS (resolution 60 000) and MS/MS (resolution 15 000) modes. To increase the depth of our analysis, we characterized both unfractionated as well as lectin-enriched proteins in our experiments. In all, we identified 1823 proteins with less than 1% false discovery rate, of which 671 proteins have not previously been reported as constituents of human urine. This data set should serve as a comprehensive reference list for future studies aimed at identification and characterization of urinary biomarkers for various diseases

A Comprehensive Map of the Human Urinary Proteome

The study of the human urinary proteome has the potential to offer significant insights into normal physiology as well as disease pathology. The information obtained from such studies could be applied to the diagnosis of various diseases. The high sensitivity, resolution, and mass accuracy of the latest generation of mass spectrometers provides an opportunity to accurately catalog the proteins present in human urine, including those present at low levels. To this end, we carried out a comprehensive analysis of human urinary proteome from healthy individuals using high-resolution Fourier transform mass spectrometry. Importantly, we used the Orbitrap for detecting ions in both MS (resolution 60 000) and MS/MS (resolution 15 000) modes. To increase the depth of our analysis, we characterized both unfractionated as well as lectin-enriched proteins in our experiments. In all, we identified 1823 proteins with less than 1% false discovery rate, of which 671 proteins have not previously been reported as constituents of human urine. This data set should serve as a comprehensive reference list for future studies aimed at identification and characterization of urinary biomarkers for various diseases

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11 février 19401940/02/11 (A69).Appartient à l’ensemble documentaire : PoitouCh

Additional file 1: of Macrophage migration inhibitory factor - a therapeutic target in gallbladder cancer

Properties of GBC cell lines used in the study. (XLS 27 kb

Additional file 8: of Macrophage migration inhibitory factor - a therapeutic target in gallbladder cancer

Representative images of MIF by immunohistochemistry. Representative sections from cholecystitis tissues (moderate staining) – (i) stained with hematoxylin and eosin; (ii) probed with anti-MIF antibody. Representative sections from gallbladder adenocarcinoma tissue (weak staining); (iii) stained with hematoxylin and eosin; (iv) probed with anti-MIF antibody. (PDF 1714 kb